Respiratory syncytial virus F glycoprotein was shown to interact with RhoA and RhoA-derived peptides which were shown to inhibit RSV infection in vitro and in a murine model. In addition, RhoA-derived peptides inhibited other viruses (Parainfluenza virus Type 3 and HIV-1) with similar glycoprotein-mediated membrane fusion mechanisms. Further studies showed that RhoA was activated during RSV infection and that inhibiting RhoA activation could alter the syncytium-forming capacity of the virus, and virus morphogenesis, resulting in less filamentous virus. Inhibiting RhoA targeting to membrane through isoprenylation inhibition, could diminish RSV replication and reduce pathogenicity in the murine model. In part, this works through shifting the assembly of RSV from cholesterol-rich lipid microdomains to other regions of the membrane.